TY - JOUR
T1 - Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions
AU - Espejo-Carpio, F. Javier
AU - De Gobba, Cristian
AU - Guadix, Antonio
AU - Guadix, Emilia M.
AU - Otte, Jeanette Anita Held
PY - 2013/10
Y1 - 2013/10
N2 - Casein and whey protein fractions from goat milk were hydrolysed by subtilisin and trypsin, individually and in combination, to release angiotensin converting enzyme (ACE)-inhibitory peptides. Selected hydrolysates were fractionated by size exclusion chromatography (SEC) and further characterised. The highest ACE-inhibitory activity was obtained from the casein fraction hydrolysed by the combination of enzymes. SEC presented 4 fractions with fraction F2 (<2.3 kDa) containing the highest concentration of peptides and the highest activity. F2 contained a number of peptides not previously identified from caprine caseins but with structural similarity to other ACE-inhibitory peptides. The most active fraction in relation to protein content was F4 with IC50 between 9.3 and 5.1μgmL-1. This fraction contained a compound tentatively identified as WY, an active dipeptide not previously reported from caseins. The high inhibitory capacity of these fractions points towards the advantage of implementing a membrane process to concentrate the most active peptides.
AB - Casein and whey protein fractions from goat milk were hydrolysed by subtilisin and trypsin, individually and in combination, to release angiotensin converting enzyme (ACE)-inhibitory peptides. Selected hydrolysates were fractionated by size exclusion chromatography (SEC) and further characterised. The highest ACE-inhibitory activity was obtained from the casein fraction hydrolysed by the combination of enzymes. SEC presented 4 fractions with fraction F2 (<2.3 kDa) containing the highest concentration of peptides and the highest activity. F2 contained a number of peptides not previously identified from caprine caseins but with structural similarity to other ACE-inhibitory peptides. The most active fraction in relation to protein content was F4 with IC50 between 9.3 and 5.1μgmL-1. This fraction contained a compound tentatively identified as WY, an active dipeptide not previously reported from caseins. The high inhibitory capacity of these fractions points towards the advantage of implementing a membrane process to concentrate the most active peptides.
U2 - 10.1016/j.idairyj.2013.04.002
DO - 10.1016/j.idairyj.2013.04.002
M3 - Journal article
SN - 0958-6946
VL - 32
SP - 175
EP - 183
JO - International Dairy Journal
JF - International Dairy Journal
IS - 2
ER -